ID A0A3B4FSX6_9CICH Unreviewed; 489 AA.
AC A0A3B4FSX6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Presenilin {ECO:0000256|RuleBase:RU361148};
DE EC=3.4.23.- {ECO:0000256|RuleBase:RU361148};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000013735.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000013735.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Probable subunit of the gamma-secretase complex, an
CC endoprotease complex that catalyzes the intramembrane cleavage of
CC integral membrane proteins such as Notch receptors.
CC {ECO:0000256|RuleBase:RU361148}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU361148}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000256|ARBA:ARBA00004489}. Cell projection, neuron projection
CC {ECO:0000256|ARBA:ARBA00004487}. Cytoplasmic granule
CC {ECO:0000256|ARBA:ARBA00004463}. Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU361148}. Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU361148}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. Synapse
CC {ECO:0000256|ARBA:ARBA00034103}.
CC -!- DOMAIN: The PAL motif is required for normal active site conformation.
CC {ECO:0000256|RuleBase:RU361148}.
CC -!- SIMILARITY: Belongs to the peptidase A22A family.
CC {ECO:0000256|ARBA:ARBA00008604, ECO:0000256|RuleBase:RU361148}.
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DR AlphaFoldDB; A0A3B4FSX6; -.
DR STRING; 303518.ENSPNYP00000013735; -.
DR Ensembl; ENSPNYT00000014078.1; ENSPNYP00000013735.1; ENSPNYG00000010399.1.
DR GeneTree; ENSGT00940000158751; -.
DR Proteomes; UP000261460; Unplaced.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0042500; F:aspartic endopeptidase activity, intramembrane cleaving; IEA:InterPro.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0016485; P:protein processing; IEA:InterPro.
DR Gene3D; 1.10.472.100; Presenilin; 1.
DR InterPro; IPR001108; Peptidase_A22A.
DR InterPro; IPR006639; Preselin/SPP.
DR InterPro; IPR042524; Presenilin_C.
DR PANTHER; PTHR10202; PRESENILIN; 1.
DR PANTHER; PTHR10202:SF18; PRESENILIN-1; 1.
DR Pfam; PF01080; Presenilin; 1.
DR PRINTS; PR01072; PRESENILIN.
DR SMART; SM00730; PSN; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU361148};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|RuleBase:RU361148}; Hydrolase {ECO:0000256|RuleBase:RU361148};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361148};
KW Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976,
KW ECO:0000256|RuleBase:RU361148}; Protease {ECO:0000256|RuleBase:RU361148};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361148};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361148}.
FT TRANSMEM 100..118
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 184..201
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 213..232
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 244..260
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 266..282
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT TRANSMEM 456..475
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361148"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 489 AA; 53975 MW; ED2BB23EE736C793 CRC64;
MANNAEDIEN NMNQQEANRS PDSTQKPQET GVPRARSRGG SAAGAGAGTG GGGDSGGGGG
GNGTSPEQNG QPPAAPAPRV VEREEEDEEE LTLKYGAKHV IMLFVPVTLC MVVVVATIKS
VSFYTQNDGQ RLIYTPFPED TDTVGQRALN SILNATIMIT VIIVMTLVLV MLYKYRCYKV
IQGWLFLSSL LLLFFFSYIY LKEVFKTYNL AMDYVTLAII IWNFGVVGMM CIHWKGPLRL
QQAYLIMISA LMALVFIKYL PEWTAWLILA VISVYDLLAV LCPKGPLRIL VETAQERNEP
IFPALIYSST MVWLVNMADT DRPNRNSTEA ASPQQEPQEA PVASPVPSSP SQDDGGFNQS
WVSQQEHRLG PLQSTEETRR EIQQMPSARP PVEEDDEERG VKLGLGDFIF YSMLVGKASA
TASGDWNTTL ACFVAILIGL CLTLLLLAIF KKALPALPIS IFFGLVFYFA TDNLVRPFMD
KLALHQFYI
//
